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The nine-subunit DNA polymerase (Pol) III* coupled to its
Volume 270,
Number 22,
Issue of June 2, pp. 13366-13377, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
III. INTERFACE BETWEEN TWO POLYMERASES AND THE CLAMP LOADER
sliding clamp is a rapid and highly processive replicating machine. The
multiple subunits are needed for the complicated task of duplicating
the Escherichia coli chromosome. In this report, Pol III* was
constituted from individual pure proteins, and its structure was
studied. Constitution of the Pol III* particle requires an ordered
addition of the subunits, and the final structure contains 14
polypeptides in the ratio
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`
&khgr;![]()
.
The structure can be summarized as being composed of two core
polymerases (![]()
) held together by a dimer of
and
one
complex clamp loader
(
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![]()
`
&khgr;![]()
)
for loading
onto DNA. At the center of the structure, the related
and
subunits form a heterotetramer upon which the two core
polymerases and clamp loader proteins assemble. The single copy nature
of the
,
`, &khgr;, and
subunits confers a structural
asymmetry with respect to the two polymerases, presumably for the
different functions of replicating the leading and lagging strands.
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